ID A0A067JRW3_JATCU Unreviewed; 402 AA.
AC A0A067JRW3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase {ECO:0000256|ARBA:ARBA00039053};
DE EC=4.4.1.14 {ECO:0000256|ARBA:ARBA00039053};
GN ORFNames=JCGZ_17795 {ECO:0000313|EMBL:KDP26637.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP26637.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP26637.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP26637.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate +
CC H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:21744,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:58360,
CC ChEBI:CHEBI:59789; EC=4.4.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00036967};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
CC {ECO:0000256|ARBA:ARBA00037888}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the alliinase family.
CC {ECO:0000256|ARBA:ARBA00006312}.
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DR EMBL; KK914893; KDP26637.1; -; Genomic_DNA.
DR RefSeq; XP_012085457.1; XM_012230067.1.
DR AlphaFoldDB; A0A067JRW3; -.
DR STRING; 180498.A0A067JRW3; -.
DR Proteomes; UP000027138; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 2.10.25.30; EGF-like, alliinase; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR006948; Alliinase_C.
DR InterPro; IPR037029; Alliinase_N_sf.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR43795:SF22; TRYPTOPHAN AMINOTRANSFERASE-RELATED PROTEIN 1; 1.
DR Pfam; PF04864; Alliinase_C; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Ethylene biosynthesis {ECO:0000256|ARBA:ARBA00022666};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT DOMAIN 35..391
FT /note="Alliinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04864"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 44799 MW; 923129F2C8D80591 CRC64;
MGGLDTAAEN GNKNSGSATN AVNGSKKVLS TDSVINLDHG DPTMFEPYWR KAGDKCTTVI
SGSDLMSYFS DIGNLCWFLE PQLSDAIKRL HRTVGNAESD DRYILVGTGS SQLCQAALYA
LSSPCGPEPI SVVCAAPYYS AYKDQIDLLH SGLYKWAGDA YAFDKDEPYI EIVTSPNNPD
GAIREAVVNR GEGKVIYDLA YYWPQYTPIT HPADYDIMLF TFSKSTGHAG SRIGWALVKD
KDVAKKMMKF MEITSIGVSK ESQLRAAKIL GVVTESCQHG VPDSENFFKY SQCLMAERWE
KLRQVVKNSA IFSLPKYPHE WCNFSEIYTE SHPAFAWLKC KEDIDCENLL RAQKLLTRGG
ERFGVGRNYV RISLLSPEEV FNLFLERLSA IKGINGQNNL NF
//
